Chapter title |
Cell-Free Assays to Measure Effects of Regulatory Ligands on AMPK
|
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Chapter number | 5 |
Book title |
AMPK
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7598-3_5 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7597-6, 978-1-4939-7598-3
|
Authors |
Fiona A. Fyffe, Simon A. Hawley, Alexander Gray, D. Grahame Hardie |
Abstract |
AMP-activated protein kinase (AMPK) is an energy sensor that is activated by increases in the cellular AMP/ATP and ADP/ATP ratios by three mechanisms: (1) allosteric activation, (2) promotion of phosphorylation at Thr172 on the α subunit by upstream kinases, and (3) inhibition of dephosphorylation of Thr172 by protein phosphatases. All of these effects are triggered by the binding of AMP or ADP at one or more of three sites on the γ subunit, where they displace ATP. AMPK is also activated by ligands that bind in the ADaM site, which is located between the α and β subunits. In this chapter we describe cell-free assays that can be used to study these varied activation mechanisms. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 3 | 60% |
Student > Ph. D. Student | 2 | 40% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 4 | 80% |
Unknown | 1 | 20% |